HEADER ONCOGENE PROTEIN 30-APR-90 5P21
TITLE REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION
TITLE 2 OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS
TITLE 3 FOR THE MECHANISM OF GTP HYDROLYSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-H-RAS P21 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ONCOGENE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.F.PAI,A.WITTINGHOFER,W.KABSCH
REVDAT 5 24-FEB-09 5P21 1 VERSN
REVDAT 4 01-APR-03 5P21 1 JRNL
REVDAT 3 20-JUL-95 5P21 1 HET
REVDAT 2 30-APR-94 5P21 1 FORMUL
REVDAT 1 15-JAN-92 5P21 0
JRNL AUTH E.F.PAI,U.KRENGEL,G.A.PETSKO,R.S.GOODY,W.KABSCH,
JRNL AUTH 2 A.WITTINGHOFER
JRNL TITL REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE
JRNL TITL 2 CONFORMATION OF H-RAS P21 AT 1.35 A RESOLUTION:
JRNL TITL 3 IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS.
JRNL REF EMBO J. V. 9 2351 1990
JRNL REFN ISSN 0261-4189
JRNL PMID 2196171
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.SCHLICHTING,S.C.ALMO,G.RAPP,K.WILSON,K.PETRATOS,
REMARK 1 AUTH 2 A.LENTFER,A.WITTINGHOFER,W.KABSCH,E.F.PAI,
REMARK 1 AUTH 3 G.A.PETSKO,R.S.GOODY
REMARK 1 TITL TIME-RESOLVED X-RAY CRYSTALLOGRAPHIC STUDY OF THE
REMARK 1 TITL 2 CONFORMATIONAL CHANGE IN HA-RAS P21 PROTEIN ON GTP
REMARK 1 TITL 3 HYDROLYSIS
REMARK 1 REF NATURE V. 345 309 1990
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.SCHERER,J.JOHN,R.LINKE,R.S.GOODY,A.WITTINGHOFER,
REMARK 1 AUTH 2 E.F.PAI,K.C.HOLMES
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 THE HUMAN C-H-RAS-ONCOGENE PRODUCT P21 COMPLEXED
REMARK 1 TITL 3 WITH GTP ANALOGUES
REMARK 1 REF J.MOL.BIOL. V. 206 257 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH E.F.PAI,W.KABSCH,U.KRENGEL,K.C.HOLMES,J.JOHN,
REMARK 1 AUTH 2 A.WITTINGHOFER
REMARK 1 TITL STRUCTURE OF THE GUANINE-NUCLEOTIDE-BINDING DOMAIN
REMARK 1 TITL 2 OF THE HA-RAS ONCOGENE PRODUCT P21 IN THE
REMARK 1 TITL 3 TRIPHOSPHATE CONFORMATION
REMARK 1 REF NATURE V. 341 209 1989
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 4
REMARK 1 AUTH I.SCHLICHTING,G.RAPP,J.JOHN,A.WITTINGHOFER,E.F.PAI,
REMARK 1 AUTH 2 R.S.GOODY
REMARK 1 TITL BIOCHEMICAL AND CRYSTALLOGRAPHIC CHARACTERIZATION
REMARK 1 TITL 2 OF A COMPLEX OF C-HA-RAS P21 AND CAGED GTP WITH
REMARK 1 TITL 3 FLASH PHOTOLYSIS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 86 7687 1989
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26806
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 2.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 61 - 65 (GLN - GLU - GLU -
REMARK 3 TYR - SER) ADOPT SEVERAL CONFORMATIONS IN THE CRYSTAL. THE
REMARK 3 COORDINATES GIVEN APPROXIMATE ONE OF THESE.
REMARK 4
REMARK 4 5P21 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 108.13333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.06667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 54.06667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 108.13333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 128 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 157 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 33 75.86 -157.25
REMARK 500 ILE A 36 -64.23 -100.39
REMARK 500 GLU A 37 123.75 -171.30
REMARK 500 SER A 65 -133.70 53.07
REMARK 500 LYS A 117 33.80 71.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 224 DISTANCE = 9.45 ANGSTROMS
REMARK 525 HOH A 243 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A 249 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A 252 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 300 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 301 DISTANCE = 10.14 ANGSTROMS
REMARK 525 HOH A 303 DISTANCE = 10.91 ANGSTROMS
REMARK 525 HOH A 304 DISTANCE = 13.77 ANGSTROMS
REMARK 525 HOH A 306 DISTANCE = 7.44 ANGSTROMS
REMARK 525 HOH A 307 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH A 311 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH A 321 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A 331 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A 366 DISTANCE = 8.86 ANGSTROMS
REMARK 525 HOH A 370 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 379 DISTANCE = 11.13 ANGSTROMS
REMARK 525 HOH A 381 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 394 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A 395 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 403 DISTANCE = 5.08 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 168 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP A 167 O2G
REMARK 620 2 GNP A 167 O2B 95.0
REMARK 620 3 HOH A 173 O 87.6 91.7
REMARK 620 4 SER A 17 OG 172.9 91.0 88.6
REMARK 620 5 THR A 35 OG1 91.3 173.4 90.5 82.8
REMARK 620 6 HOH A 172 O 97.3 88.0 175.0 86.5 89.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 168
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 167
DBREF 5P21 A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES 2 A 166 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES 3 A 166 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 166 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES 5 A 166 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES 6 A 166 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES 7 A 166 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES 8 A 166 ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES 9 A 166 ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES 10 A 166 CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES 11 A 166 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES 12 A 166 THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES 13 A 166 TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET MG A 168 1
HET GNP A 167 32
HETNAM MG MAGNESIUM ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL 2 MG MG 2+
FORMUL 3 GNP C10 H17 N6 O13 P3
FORMUL 4 HOH *211(H2 O)
HELIX 1 HA LYS A 16 GLN A 25 1 10
HELIX 2 HB SER A 65 THR A 74 1RES 65-67 IN 3/10 CONF 10
HELIX 3 HC THR A 87 VAL A 103 1BREAK AT ASP 92 17
HELIX 4 HD SER A 127 TYR A 137 1 11
HELIX 5 HE VAL A 152 ARG A 164 1 13
SHEET 1 S1 6 GLU A 37 ILE A 46 0
SHEET 2 S1 6 GLU A 49 THR A 58 -1 O LEU A 53 N LYS A 42
SHEET 3 S1 6 THR A 2 VAL A 9 1 N LEU A 6 O ASP A 54
SHEET 4 S1 6 GLY A 77 ALA A 83 1 N LEU A 79 O VAL A 7
SHEET 5 S1 6 MET A 111 ASN A 116 1 N VAL A 114 O CYS A 80
SHEET 6 S1 6 TYR A 141 GLU A 143 1 N ILE A 142 O LEU A 113
LINK MG MG A 168 O2G GNP A 167 1555 1555 2.20
LINK MG MG A 168 O2B GNP A 167 1555 1555 2.22
LINK MG MG A 168 O HOH A 173 1555 1555 2.23
LINK MG MG A 168 OG SER A 17 1555 1555 2.26
LINK MG MG A 168 OG1 THR A 35 1555 1555 2.26
LINK MG MG A 168 O HOH A 172 1555 1555 2.30
SITE 1 AC1 5 SER A 17 THR A 35 GNP A 167 HOH A 172
SITE 2 AC1 5 HOH A 173
SITE 1 AC2 28 GLY A 12 GLY A 13 VAL A 14 GLY A 15
SITE 2 AC2 28 LYS A 16 SER A 17 ALA A 18 PHE A 28
SITE 3 AC2 28 VAL A 29 ASP A 30 TYR A 32 PRO A 34
SITE 4 AC2 28 THR A 35 GLY A 60 ASN A 116 LYS A 117
SITE 5 AC2 28 ASP A 119 SER A 145 ALA A 146 LYS A 147
SITE 6 AC2 28 MG A 168 HOH A 170 HOH A 172 HOH A 173
SITE 7 AC2 28 HOH A 175 HOH A 187 HOH A 281 HOH A 366
CRYST1 40.300 40.300 162.200 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024814 0.014326 0.000000 0.00000
SCALE2 0.000000 0.028653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006165 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
